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Article ; Online: Multiplex Serology for Sensitive and Specific Flavivirus IgG Detection: Addition of Envelope Protein Domain III to NS1 Increases Sensitivity for Tick-Borne Encephalitis Virus IgG Detection.

Valle, Coralie / Shrestha, Sandhya / Godeke, Gert-Jan / Hoogerwerf, Marieke N / Reimerink, Johan / Eggink, Dirk / Reusken, Chantal

Viruses

2024 Volume 16, Issue 2

Abstract: Tick-borne encephalitis is a vaccine-preventable disease of concern for public health in large parts of Europe, with EU notification rates increasing since 2018. It is caused by the orthoflavivirus tick-borne encephalitis virus (TBEV) and a diagnosis of ... ...

Abstract	Tick-borne encephalitis is a vaccine-preventable disease of concern for public health in large parts of Europe, with EU notification rates increasing since 2018. It is caused by the orthoflavivirus tick-borne encephalitis virus (TBEV) and a diagnosis of infection is mainly based on serology due to its short viremic phase, often before symptom onset. The interpretation of TBEV serology is hampered by a history of orthoflavivirus vaccination and by previous infections with related orthoflaviviruses. Here, we sought to improve TBEV sero-diagnostics using an antigen combination of in-house expressed NS1 and EDIII in a multiplex, low-specimen-volume set-up for the detection of immune responses to TBEV and other clinically important orthoflaviviruses (i.e., West Nile virus, dengue virus, Japanese encephalitis virus, Usutu virus and Zika virus). We show that the combined use of NS1 and EDIII results in both a specific and sensitive test for the detection of TBEV IgG for patient diagnostics, vaccination responses and in seroprevalence studies. This novel approach potentially allows for a low volume-based, simultaneous analysis of IgG responses to a range of orthoflaviviruses with overlapping geographic circulations and clinical manifestations.
MeSH term(s)	Humans ; Encephalitis Viruses, Tick-Borne ; Protein Domains ; Seroepidemiologic Studies ; Antibodies, Viral ; Flavivirus Infections/diagnosis ; Encephalitis, Tick-Borne ; Encephalitis, Viral ; Immunoglobulin G ; Zika Virus ; Zika Virus Infection
Chemical Substances	Antibodies, Viral ; Immunoglobulin G
Language	English
Publishing date	2024-02-13
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v16020286
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Article: Neuroprotective effects of G9a inhibition through modulation of peroxisome-proliferator activator receptor gamma-dependent pathways by miR-128.

Bellver-Sanchis, Aina / Ávila-López, Pedro A / Tic, Iva / Valle-García, David / Ribalta-Vilella, Marta / Labrador, Luis / Banerjee, Deb Ranjan / Guerrero, Ana / Casadesus, Gemma / Poulard, Coralie / Pallàs, Mercè / Griñán-Ferré, Christian

Neural regeneration research

2024 Volume 19, Issue 11, Page(s) 2532–2542

Abstract: JOURNAL/nrgr/04.03/01300535-202419110-00033/figure1/v/2024-03-08T184507Z/r/image-tiff Dysregulation of G9a, a histone-lysine N-methyltransferase, has been observed in Alzheimer's disease and has been correlated with increased levels of chronic ... ...

Abstract	JOURNAL/nrgr/04.03/01300535-202419110-00033/figure1/v/2024-03-08T184507Z/r/image-tiff Dysregulation of G9a, a histone-lysine N-methyltransferase, has been observed in Alzheimer's disease and has been correlated with increased levels of chronic inflammation and oxidative stress. Likewise, microRNAs are involved in many biological processes and diseases playing a key role in pathogenesis, especially in multifactorial diseases such as Alzheimer's disease. Therefore, our aim has been to provide partial insights into the interconnection between G9a, microRNAs, oxidative stress, and neuroinflammation. To better understand the biology of G9a, we compared the global microRNA expression between senescence-accelerated mouse-prone 8 (SAMP8) control mice and SAMP8 treated with G9a inhibitor UNC0642. We found a downregulation of miR-128 after a G9a inhibition treatment, which interestingly binds to the 3' untranslated region (3'-UTR) of peroxisome-proliferator activator receptor γ (PPARG) mRNA. Accordingly, Pparg gene expression levels were higher in the SAMP8 group treated with G9a inhibitor than in the SAMP8 control group. We also observed modulation of oxidative stress responses might be mainly driven Pparg after G9a inhibitor. To confirm these antioxidant effects, we treated primary neuron cell cultures with hydrogen peroxide as an oxidative insult. In this setting, treatment with G9a inhibitor increases both cell survival and antioxidant enzymes. Moreover, up-regulation of PPARγ by G9a inhibitor could also increase the expression of genes involved in DNA damage responses and apoptosis. In addition, we also described that the PPARγ/AMPK axis partially explains the regulation of autophagy markers expression. Finally, PPARγ/GADD45α potentially contributes to enhancing synaptic plasticity and neurogenesis after G9a inhibition. Altogether, we propose that pharmacological inhibition of G9a leads to a neuroprotective effect that could be due, at least in part, by the modulation of PPARγ-dependent pathways by miR-128.
Language	English
Publishing date	2024-01-08
Publishing country	India
Document type	Journal Article
ZDB-ID	2388460-5
ISSN	1876-7958 ; 1673-5374
ISSN (online)	1876-7958
ISSN	1673-5374
DOI	10.4103/1673-5374.393102
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Article ; Online: Structure and Sequence Requirements for RNA Capping at the Venezuelan Equine Encephalitis Virus RNA 5' End.

Ortega Granda, Oney / Valle, Coralie / Shannon, Ashleigh / Decroly, Etienne / Canard, Bruno / Coutard, Bruno / Rabah, Nadia

Journal of virology

2021 Volume 95, Issue 15, Page(s) e0077721

Abstract: Venezuelan equine encephalitis virus (VEEV) is a reemerging arthropod-borne virus causing encephalitis in humans and domesticated animals. VEEV possesses a positive single-stranded RNA genome capped at its 5' end. The capping process is performed by the ... ...

Abstract	Venezuelan equine encephalitis virus (VEEV) is a reemerging arthropod-borne virus causing encephalitis in humans and domesticated animals. VEEV possesses a positive single-stranded RNA genome capped at its 5' end. The capping process is performed by the nonstructural protein nsP1, which bears methyl and guanylyltransferase activities. The capping reaction starts with the methylation of GTP. The generated m
MeSH term(s)	Animals ; Encephalitis Virus, Venezuelan Equine/genetics ; Encephalomyelitis, Venezuelan Equine/pathology ; Encephalomyelitis, Venezuelan Equine/virology ; Horses ; Humans ; Methyltransferases/metabolism ; Nucleic Acid Conformation ; Nucleotidyltransferases/metabolism ; RNA Caps/genetics ; RNA, Viral/genetics ; Viral Nonstructural Proteins/genetics ; Viral Nonstructural Proteins/metabolism ; Virus Replication/genetics
Chemical Substances	RNA Caps ; RNA, Viral ; Viral Nonstructural Proteins ; Methyltransferases (EC 2.1.1.-) ; Nucleotidyltransferases (EC 2.7.7.-) ; guanylyltransferase (EC 2.7.7.-)
Language	English
Publishing date	2021-07-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00777-21
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Article ; Online: Drugs against SARS‐CoV ‐2

Valle, Coralie / Martin, Baptiste / Touret, Franck / Shannon, Ashleigh / Canard, Bruno / Guillemot, Jean‐Claude / Coutard, Bruno / Decroly, Etienne

Reviews in Medical Virology ; ISSN 1052-9276 1099-1654

What do we know about their mode of action?

2020

Keywords	Virology ; Infectious Diseases ; covid19
Language	English
Publisher	Wiley
Publishing country	us
Document type	Article ; Online
DOI	10.1002/rmv.2143
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Article ; Online: La protéine L du virus Ébola porte une nouvelle activité enzymatique impliquée dans la méthylation interne des ARN.

Martin, Baptiste / Valle, Coralie / Coutard, Bruno / Canard, Bruno / Debart, Françoise / Decroly, Étienne

Medecine sciences : M/S

2018 Volume 34, Issue 11, Page(s) 919–921

Title translation	Ebola virus L protein harbors a new enzymatic activity involved in the internal methylation of RNAs.
MeSH term(s)	Animals ; Ebolavirus/enzymology ; Hemorrhagic Fever, Ebola/virology ; Humans ; Methylation ; Methyltransferases/chemistry ; Methyltransferases/physiology ; Polyribonucleotide Nucleotidyltransferase/chemistry ; Polyribonucleotide Nucleotidyltransferase/physiology ; Protein Conformation ; Protein Domains ; RNA/metabolism ; RNA Replicase/chemistry ; RNA Replicase/physiology ; Viral Proteins/chemistry ; Viral Proteins/physiology
Chemical Substances	Viral Proteins ; RNA (63231-63-0) ; Methyltransferases (EC 2.1.1.-) ; RNA Replicase (EC 2.7.7.48) ; Polyribonucleotide Nucleotidyltransferase (EC 2.7.7.8)
Language	French
Publishing date	2018-12-10
Publishing country	France
Document type	News
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/2018230
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Article ; Online: The C-Terminal Domain of the Sudan Ebolavirus L Protein Is Essential for RNA Binding and Methylation.

Valle, Coralie / Martin, Baptiste / Debart, Françoise / Vasseur, Jean-Jacques / Imbert, Isabelle / Canard, Bruno / Coutard, Bruno / Decroly, Etienne

Journal of virology

2020 Volume 94, Issue 12

Abstract: The large (L) protein of Ebola virus is a key protein for virus replication. Its N-terminal region harbors the RNA-dependent RNA polymerase activity, and its C terminus contains a cap assembling line composed of a capping domain and a methyltransferase ... ...

Abstract	The large (L) protein of Ebola virus is a key protein for virus replication. Its N-terminal region harbors the RNA-dependent RNA polymerase activity, and its C terminus contains a cap assembling line composed of a capping domain and a methyltransferase domain (MTase) followed by a C-terminal domain (CTD) of unknown function. The L protein MTase catalyzes methylation at the 2'-O and N-7 positions of the cap structures. In addition, the MTase of Ebola virus can induce cap-independent internal adenosine 2'-
MeSH term(s)	Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Ebolavirus/genetics ; Ebolavirus/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression ; Gene Expression Regulation ; Host-Pathogen Interactions/genetics ; Humans ; Methylation ; Methyltransferases/genetics ; Methyltransferases/metabolism ; Models, Molecular ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Domains ; Protein Interaction Domains and Motifs ; RNA Replicase/genetics ; RNA Replicase/metabolism ; RNA, Viral/genetics ; RNA, Viral/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid ; Signal Transduction ; Viral Nonstructural Proteins/genetics ; Viral Nonstructural Proteins/metabolism ; Virus Replication
Chemical Substances	RNA, Viral ; Recombinant Proteins ; Viral Nonstructural Proteins ; Methyltransferases (EC 2.1.1.-) ; RNA Replicase (EC 2.7.7.48)
Keywords	covid19
Language	English
Publishing date	2020-06-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00520-20
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Article ; Online: Drugs against SARS-CoV-2: What do we know about their mode of action?

Valle, Coralie / Martin, Baptiste / Touret, Franck / Shannon, Ashleigh / Canard, Bruno / Guillemot, Jean-Claude / Coutard, Bruno / Decroly, Etienne

Reviews in medical virology

2020 Volume 30, Issue 6, Page(s) 1–10

Abstract: The health emergency caused by the recent Covid-19 pandemic highlights the need to identify effective treatments against the virus causing this disease (SARS-CoV-2). The first clinical trials have been testing repurposed drugs that show promising anti- ... ...

Abstract	The health emergency caused by the recent Covid-19 pandemic highlights the need to identify effective treatments against the virus causing this disease (SARS-CoV-2). The first clinical trials have been testing repurposed drugs that show promising anti-SARS-CoV-2 effects in cultured cells. Although more than 2400 clinical trials are already under way, the actual number of tested compounds is still limited to approximately 20, alone or in combination. In addition, knowledge on their mode of action (MoA) is currently insufficient. Their first results reveal some inconsistencies and contradictory results and suggest that cohort size and quality of the control arm are two key issues for obtaining rigorous and conclusive results. Moreover, the observed discrepancies might also result from differences in the clinical inclusion criteria, including the possibility of early treatment that may be essential for therapy efficacy in patients with Covid-19. Importantly, efforts should also be made to test new compounds with a documented MoA against SARS-CoV-2 in clinical trials. Successful treatment will probably be based on multitherapies with antiviral compounds that target different steps of the virus life cycle. Moreover, a multidisciplinary approach that combines artificial intelligence, compound docking, and robust in vitro and in vivo assays will accelerate the development of new antiviral molecules. Finally, large retrospective studies on hospitalized patients are needed to evaluate the different treatments with robust statistical tools and to identify the best treatment for each Covid-19 stage. This review describes different candidate antiviral strategies for Covid-19, by focusing on their mechanism of action.
MeSH term(s)	Antiviral Agents/pharmacology ; Antiviral Agents/therapeutic use ; COVID-19/virology ; Combined Modality Therapy ; Disease Management ; Disease Susceptibility ; Drug Development ; Drug Repositioning ; Host-Pathogen Interactions ; Humans ; SARS-CoV-2/drug effects ; SARS-CoV-2/physiology ; Treatment Outcome ; COVID-19 Drug Treatment
Chemical Substances	Antiviral Agents
Keywords	covid19
Language	English
Publishing date	2020-08-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1086043-5
ISSN	1099-1654 ; 1052-9276
ISSN (online)	1099-1654
ISSN	1052-9276
DOI	10.1002/rmv.2143
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Article ; Online: First insights into the structural features of Ebola virus methyltransferase activities.

Valle, Coralie / Martin, Baptiste / Ferron, François / Roig-Zamboni, Véronique / Desmyter, Aline / Debart, Françoise / Vasseur, Jean-Jacques / Canard, Bruno / Coutard, Bruno / Decroly, Etienne

Nucleic acids research

2021 Volume 49, Issue 3, Page(s) 1737–1748

Abstract: The Ebola virus is a deadly human pathogen responsible for several outbreaks in Africa. Its genome encodes the 'large' L protein, an essential enzyme that has polymerase, capping and methyltransferase activities. The methyltransferase activity leads to ... ...

Abstract	The Ebola virus is a deadly human pathogen responsible for several outbreaks in Africa. Its genome encodes the 'large' L protein, an essential enzyme that has polymerase, capping and methyltransferase activities. The methyltransferase activity leads to RNA co-transcriptional modifications at the N7 position of the cap structure and at the 2'-O position of the first transcribed nucleotide. Unlike other Mononegavirales viruses, the Ebola virus methyltransferase also catalyses 2'-O-methylation of adenosines located within the RNA sequences. Herein, we report the crystal structure at 1.8 Å resolution of the Ebola virus methyltransferase domain bound to a fragment of a camelid single-chain antibody. We identified structural determinants and key amino acids specifically involved in the internal adenosine-2'-O-methylation from cap-related methylations. These results provide the first high resolution structure of an ebolavirus L protein domain, and the framework to investigate the effects of epitranscriptomic modifications and to design possible antiviral drugs against the Filoviridae family.
MeSH term(s)	Catalytic Domain ; Crystallography, X-Ray ; Ebolavirus/enzymology ; Methyltransferases/chemistry ; Methyltransferases/genetics ; Methyltransferases/metabolism ; Models, Molecular ; Mutation ; Protein Conformation, alpha-Helical ; Single-Domain Antibodies/chemistry ; Viral Proteins/chemistry ; Viral Proteins/genetics ; Viral Proteins/metabolism
Chemical Substances	Single-Domain Antibodies ; Viral Proteins ; Methyltransferases (EC 2.1.1.-)
Language	English
Publishing date	2021-01-27
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkaa1276
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Article ; Online: Design, Synthesis and Discovery of N,N'-Carbazoyl-aryl-urea Inhibitors of Zika NS5 Methyltransferase and Virus Replication.

Spizzichino, Sharon / Mattedi, Giulio / Lauder, Kate / Valle, Coralie / Aouadi, Wahiba / Canard, Bruno / Decroly, Etienne / Kaptein, Suzanne J F / Neyts, Johan / Graham, Carl / Sule, Zakary / Barlow, David J / Silvestri, Romano / Castagnolo, Daniele

ChemMedChem

2020 Volume 15, Issue 4, Page(s) 385–390

Abstract: The recent outbreaks of Zika virus (ZIKV) infection worldwide make the discovery of novel antivirals against flaviviruses a research priority. This work describes the identification of novel inhibitors of ZIKV through a structure-based virtual screening ... ...

Abstract	The recent outbreaks of Zika virus (ZIKV) infection worldwide make the discovery of novel antivirals against flaviviruses a research priority. This work describes the identification of novel inhibitors of ZIKV through a structure-based virtual screening approach using the ZIKV NS5-MTase. A novel series of molecules with a carbazoyl-aryl-urea structure has been discovered and a library of analogues has been synthesized. The new compounds inhibit ZIKV MTase with IC
MeSH term(s)	Antiviral Agents/chemical synthesis ; Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Dose-Response Relationship, Drug ; Drug Discovery ; Methyltransferases/antagonists & inhibitors ; Methyltransferases/metabolism ; Microbial Sensitivity Tests ; Models, Molecular ; Molecular Structure ; Structure-Activity Relationship ; Urea/analogs & derivatives ; Urea/chemistry ; Urea/pharmacology ; Virus Replication/drug effects ; Zika Virus/drug effects ; Zika Virus/enzymology
Chemical Substances	Antiviral Agents ; Urea (8W8T17847W) ; Methyltransferases (EC 2.1.1.-)
Language	English
Publishing date	2020-01-07
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2218496-X
ISSN	1860-7187 ; 1860-7179
ISSN (online)	1860-7187
ISSN	1860-7179
DOI	10.1002/cmdc.201900533
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Article ; Online: Synthesis and biological evaluation of novel flexible nucleoside analogues that inhibit flavivirus replication in vitro.

Thames, Joy E / Waters, Charles D / Valle, Coralie / Bassetto, Marcella / Aouadi, Wahiba / Martin, Baptiste / Selisko, Barbara / Falat, Arissa / Coutard, Bruno / Brancale, Andrea / Canard, Bruno / Decroly, Etienne / Seley-Radtke, Katherine L

Bioorganic & medicinal chemistry

2020 Volume 28, Issue 22, Page(s) 115713

Abstract: Flaviviruses, such as Dengue (DENV) and Zika (ZIKV) viruses, represent a severe health burden. There are currently no FDA-approved treatments, and vaccines against most flaviviruses are still lacking. We have developed several flexible analogues (" ... ...

Abstract	Flaviviruses, such as Dengue (DENV) and Zika (ZIKV) viruses, represent a severe health burden. There are currently no FDA-approved treatments, and vaccines against most flaviviruses are still lacking. We have developed several flexible analogues ("fleximers") of the FDA-approved nucleoside Acyclovir that exhibit activity against various RNA viruses, demonstrating their broad-spectrum potential. The current study reports activity against DENV and Yellow Fever Virus (YFV), particularly for compound 1. Studies to elucidate the mechanism of action suggest the flex-analogue triphosphates, especially 1-TP, inhibit DENV and ZIKV methyltransferases, and a secondary, albeit weak, effect on the DENV RNA-dependent RNA polymerase was observed at high concentrations. The results of these studies are reported herein.
MeSH term(s)	Antiviral Agents/chemical synthesis ; Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Dose-Response Relationship, Drug ; Flavivirus/drug effects ; Microbial Sensitivity Tests ; Models, Molecular ; Molecular Structure ; Nucleosides/chemical synthesis ; Nucleosides/chemistry ; Nucleosides/pharmacology ; Structure-Activity Relationship ; Virus Replication/drug effects
Chemical Substances	Antiviral Agents ; Nucleosides
Keywords	covid19
Language	English
Publishing date	2020-08-31
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1161284-8
ISSN	1464-3391 ; 0968-0896
ISSN (online)	1464-3391
ISSN	0968-0896
DOI	10.1016/j.bmc.2020.115713
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